PMID- 9456326
OWN - NLM
STAT- MEDLINE
DCOM- 19980309
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 140
IP  - 3
DP  - 1998 Feb 9
TI  - beta-Spectrin is colocalized with both voltage-gated sodium channels and ankyrinG 
      at the adult rat neuromuscular junction.
PG  - 675-84
AB  - Voltage-gated sodium channels (VGSCs) are concentrated in the depths of the 
      postsynaptic folds at mammalian neuromuscular junctions (NMJs) where they 
      facilitate action potential generation during neuromuscular transmission. At the 
      nodes of Ranvier and the axon hillocks of central neurons, VGSCs are associated 
      with the cytoskeletal proteins, beta-spectrin and ankyrin, which may help to 
      maintain the high local density of VGSCs. Here we show in skeletal muscle, using 
      immunofluorescence, that beta-spectrin is precisely colocalized with both VGSCs 
      and ankyrinG, the nodal isoform of ankyrin. In en face views of rat NMJs, 
      acetylcholine receptors (AChRs), and utrophin immunolabeling are organized in 
      distinctive linear arrays corresponding to the crests of the postsynaptic folds. 
      In contrast, beta-spectrin, VGSCs, and ankyrinG have a punctate distribution that 
      extends laterally beyond the AChRs, consistent with a localization in the depths 
      of the folds. Double antibody labeling shows that beta-spectrin is precisely 
      colocalized with both VGSCs and ankyrinG at the NMJ. Furthermore, quantification 
      of immunofluorescence in labeled transverse sections reveals that beta-spectrin 
      is also concentrated in perijunctional regions, in parallel with an increase in 
      labeling of VGSCs and ankyrinG, but not of dystrophin. These observations suggest 
      that interactions with beta-spectrin and ankyrinG help to maintain the 
      concentration of VGSCs at the NMJ and that a common mechanism exists throughout 
      the nervous system for clustering VGSCs at a high density.
FAU - Wood, S J
AU  - Wood SJ
AD  - School of Neurosciences, The Medical School, University of Newcastle upon Tyne 
      NE2 4HH, United Kingdom. s.j.wood@bristol.ac.uk
FAU - Slater, C R
AU  - Slater CR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Ankyrins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Dystrophin)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, Cholinergic)
RN  - 0 (Sodium Channels)
RN  - 0 (Utrophin)
RN  - 12634-43-4 (Spectrin)
SB  - IM
MH  - Animals
MH  - Ankyrins/*analysis
MH  - Cytoskeletal Proteins/analysis
MH  - Dystrophin/analysis
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Ion Channel Gating
MH  - Membrane Proteins/analysis
MH  - Muscle, Skeletal/chemistry
MH  - Neuromuscular Junction/*chemistry/ultrastructure
MH  - Rats
MH  - Receptors, Cholinergic/analysis
MH  - Sodium Channels/*analysis
MH  - Spectrin/*analysis
MH  - Utrophin
PMC - PMC2140176
EDAT- 1998/03/14 00:00
MHDA- 1998/03/14 00:01
PMCR- 1998/08/09
CRDT- 1998/03/14 00:00
PHST- 1998/03/14 00:00 [pubmed]
PHST- 1998/03/14 00:01 [medline]
PHST- 1998/03/14 00:00 [entrez]
PHST- 1998/08/09 00:00 [pmc-release]
AID - 10.1083/jcb.140.3.675 [doi]
PST - ppublish
SO  - J Cell Biol. 1998 Feb 9;140(3):675-84. doi: 10.1083/jcb.140.3.675.